Abstract
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO⋯HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.
Original language | English |
---|---|
Pages (from-to) | 7868-7869 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 132 |
Issue number | 23 |
DOIs | |
Publication status | Published - 2010 Jun 16 |
All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry